ID   BISC_CERSP              Reviewed;         744 AA.
AC   P54934;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Biotin sulfoxide reductase;
DE            EC=1.-.-.-;
DE   AltName: Full=BDS reductase;
DE   AltName: Full=BSO reductase;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=f. sp. denitrificans IL106;
RX   PubMed=7733660; DOI=10.1006/abbi.1995.1236;
RA   Pollock V.V., Barber M.J.;
RT   "Molecular cloning and expression of biotin sulfoxide reductase from
RT   Rhodobacter sphaeroides forma sp. denitrificans.";
RL   Arch. Biochem. Biophys. 318:322-332(1995).
CC   -!- FUNCTION: This enzyme may serve as a scavenger, allowing the cell to
CC       utilize biotin sulfoxide as a biotin source. It reduces a spontaneous
CC       oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to
CC       biotin (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC       bis-MGD) cofactor per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; U08189; AAA74739.1; -; Genomic_DNA.
DR   PIR; S65669; S65669.
DR   AlphaFoldDB; P54934; -.
DR   SMR; P54934; -.
DR   BioCyc; MetaCyc:MON-181; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006658; BisC.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR00509; bisC_fam; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Molybdenum; Oxidoreductase.
FT   CHAIN           1..744
FT                   /note="Biotin sulfoxide reductase"
FT                   /id="PRO_0000063220"
FT   BINDING         121
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   744 AA;  80266 MW;  731A933E95358A19 CRC64;
     MGVEPFAHDP APSELIHSVP ACGSPERRVM RPMVREGWLA DRQHSDRRGR GRERFLPVSW
     DAALDLVAGE IRRVSADHGN AAIFAGSYGW TSCGRFHHAS TLLKRMLNLV GGFTGHVDTY
     SIAAGPVILR HTLGDDRACG GQANTLDSIA EHSQTLVVFG AMSPRTAQSE AGGIGAHHLE
     TYLRRIVERG VRVILVSPLK DDLPDWVAAE WWPIRPNTDT ALMLGLAGEI VRSGRQDSDF
     LARCTSGSEL YLAYLRGEGD GRPKDAEWAS TITGLPAEAI RALAGDLPRT RSMLTVSWSL
     QRAHHGEQPF WAALGLAAVI GQIGRPGGGV GYGYGSLGGV GAPFTIGKSP AMSQLSKPIN
     SFIPVARISD MLLNPGGPYS YEGEDRRYPD IRLVYWSGGN PFHHHQDLNR LSEAWTRPET
     IIVQDPMFTA TAKRADIVLP ASTSIERNDL AGNKRSDFIL AMGQAIAPLG EARSDFDIFN
     ALSGKLGVAA AFNEGRDEMG WIRHLYEESR NHAQRHHHFE MPDFETFWAQ GHAPCPVQRD
     HTYLAAFRED PGAHPLDTES GLIVLGSATL ARLGYADCGP HPAWIEPAEW LGKAQAGELH
     LISHQPKGRL HSQLETAEAS LAGKREGRDE VMLHPDDASV RGIADGQTVR LWNARGACLA
     TAQVTDSVAA GVAILPTGAW FTPAEAEGPE LSGNPNVLTL DIGSSAFGQG CSAHTCLVRI
     EAHAGDAGDA VRIYDAHLAA ILPT